Intramembrane Proteolysis by Signal Peptide Peptidases: A Comparative Discussion of GXGD-type Aspartyl Proteases
| Autor: | Harald Steiner, Christian Haass, Regina Fluhrer |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Signal peptide
Proteases Amino Acid Motifs Molecular Sequence Data Biology Biochemistry Deubiquitinating enzyme Cell membrane parasitic diseases Retroviral aspartyl protease medicine Animals Aspartic Acid Endopeptidases Humans ddc:610 Amino Acid Sequence Molecular Biology Peptide sequence chemistry [Aspartic Acid Endopeptidases] enzymology [Cell Membrane] Cell Membrane Minireviews Cell Biology metabolism [Aspartic Acid Endopeptidases] medicine.anatomical_structure Membrane protein ddc:540 signal peptide peptidase biology.protein Protein Processing Post-Translational Signal peptide peptidase |
| Zdroj: | The journal of biological chemistry 284(21), 13975-13979 (2009). doi:10.1074/jbc.R800040200 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.r800040200 |
| Popis: | Intramembrane-cleaving proteases are required for reverse signaling and membrane protein degradation. A major class of these proteases is represented by the GXGD-type aspartyl proteases. GXGD describes a novel signature sequence that distinguishes these proteases from conventional aspartyl proteases. Members of the family of the GXGD-type aspartyl proteases are the Alzheimer disease-related γ-secretase, the signal peptide peptidases and their homologs, and the bacterial type IV prepilin peptidases. We will describe the major biochemical and functional properties of the signal peptide peptidases and their relatives. We then compare these properties with those of γ-secretase and discuss common mechanisms but also point out a number of substantial differences. |
| Databáze: | OpenAIRE |
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